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LPS interactions with immobilized and soluble antimicrobial peptides.

Gustafsson, Anna LU ; Olin, Anders LU and Ljunggren, Lennart (2010) In Scandinavian Journal of Clinical and Laboratory Investigation Apr 7. p.194-200
Abstract
Abstract A promising approach in sepsis therapy is the use of peptides truncated from serum- and membrane-proteins with binding domains for LPS: antimicrobial peptides (AMPs). AMPs can be useful in combination with conventional antibiotics to increase killing and neutralize LPS. Although many AMPs show a high specificity towards bacterial membranes, they can also exhibit toxicity, i.e. non-specific membrane lysis, of mammalian cells such as erythrocytes and therefore, unsuitable as systemic drugs. A way to overcome this problem may be an extracorporeal therapy with immobilized peptides. This study will compare neutralization of LPS using different AMPs in solution and when immobilized on to solid phases. The peptides ability to neutralize... (More)
Abstract A promising approach in sepsis therapy is the use of peptides truncated from serum- and membrane-proteins with binding domains for LPS: antimicrobial peptides (AMPs). AMPs can be useful in combination with conventional antibiotics to increase killing and neutralize LPS. Although many AMPs show a high specificity towards bacterial membranes, they can also exhibit toxicity, i.e. non-specific membrane lysis, of mammalian cells such as erythrocytes and therefore, unsuitable as systemic drugs. A way to overcome this problem may be an extracorporeal therapy with immobilized peptides. This study will compare neutralization of LPS using different AMPs in solution and when immobilized on to solid phases. The peptides ability to neutralize LPS-induced cytokine release in whole blood will also be tested. The peptides are truncated derivates from the known AMPs LL-37, SC4, BPI, S3Delta and CEME. Two different methods were used to immobilize peptides, biomolecular interaction analysis, and Pierce SulfoLink Coupling Gel. To investigate LPS binding in solution the LAL test was used. After whole blood incubation with LPS and AMPs ELISA was used to measure TNFalpha, IL-1beta and IL-6 production. The results suggest that immobilization of antimicrobial peptides does not inhibit their capacity to neutralize LPS, although there are differences between the peptides tested. Thus, peptides derived from LL-37 and CEME were more efficient both in LPS binding and neutralizing LPS-induced cytokine production. (Less)
Please use this url to cite or link to this publication:
author
; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Scandinavian Journal of Clinical and Laboratory Investigation
volume
Apr 7
pages
194 - 200
publisher
Informa Healthcare
external identifiers
  • wos:000276814500008
  • pmid:20233038
  • scopus:77951490780
  • pmid:20233038
ISSN
1502-7686
DOI
10.3109/00365511003663622
language
English
LU publication?
yes
id
c0de80a0-fe47-4c2b-813f-e4920ee226ee (old id 1582056)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/20233038?dopt=Abstract
date added to LUP
2016-04-04 09:32:16
date last changed
2025-04-04 14:14:44
@article{c0de80a0-fe47-4c2b-813f-e4920ee226ee,
  abstract     = {{Abstract A promising approach in sepsis therapy is the use of peptides truncated from serum- and membrane-proteins with binding domains for LPS: antimicrobial peptides (AMPs). AMPs can be useful in combination with conventional antibiotics to increase killing and neutralize LPS. Although many AMPs show a high specificity towards bacterial membranes, they can also exhibit toxicity, i.e. non-specific membrane lysis, of mammalian cells such as erythrocytes and therefore, unsuitable as systemic drugs. A way to overcome this problem may be an extracorporeal therapy with immobilized peptides. This study will compare neutralization of LPS using different AMPs in solution and when immobilized on to solid phases. The peptides ability to neutralize LPS-induced cytokine release in whole blood will also be tested. The peptides are truncated derivates from the known AMPs LL-37, SC4, BPI, S3Delta and CEME. Two different methods were used to immobilize peptides, biomolecular interaction analysis, and Pierce SulfoLink Coupling Gel. To investigate LPS binding in solution the LAL test was used. After whole blood incubation with LPS and AMPs ELISA was used to measure TNFalpha, IL-1beta and IL-6 production. The results suggest that immobilization of antimicrobial peptides does not inhibit their capacity to neutralize LPS, although there are differences between the peptides tested. Thus, peptides derived from LL-37 and CEME were more efficient both in LPS binding and neutralizing LPS-induced cytokine production.}},
  author       = {{Gustafsson, Anna and Olin, Anders and Ljunggren, Lennart}},
  issn         = {{1502-7686}},
  language     = {{eng}},
  pages        = {{194--200}},
  publisher    = {{Informa Healthcare}},
  series       = {{Scandinavian Journal of Clinical and Laboratory Investigation}},
  title        = {{LPS interactions with immobilized and soluble antimicrobial peptides.}},
  url          = {{http://dx.doi.org/10.3109/00365511003663622}},
  doi          = {{10.3109/00365511003663622}},
  volume       = {{Apr 7}},
  year         = {{2010}},
}